Earlier it was reported that methanol, 2-chloroethanol, and trifluoroethanol affected the circular dichroic (CD) spectrum of reduced lysozyme in a manner consistent with increases in Alpha helix and loss of Beta-structure. However, separation of polymer from monomer by gel filtration showed that only the polymer contributed to these changes and that the monomer either remained unchanged or deteriorated further. Within the past year, it has been found that methanol can be explored at much higher concentrations than previously found possible, where the limiting factor was the extensive polymer formation. Thus, at 40% methanol (vol/vol) substantial amounts of monomer have now been isolated and are found to remain unchanged in CD behavior, compared to that of reduced lysozyme in aqueous solution. These findings suggest, contrary to the more popular concept, that hydrophobic interactions may contribute little or nothing in the early stages of the process by which the protein chain assumes native secondary structure.